pauling linus corey robert (2 risultati)

1st Edition. FIRST EDITION OF LINUS PAULING AND ROBERT COREY'S FIRST ANNOUNCEMENT OF THEIR SEMINAL MOLECULAR BIOLOGY FINDINGS REGARDING THE THEORETICAL ALPHA AND GAMMA HELIXES, TWO CONFIGURATIONS OF THE ARRANGEMENT OF ATOMS IN PROTEINS. The authors "must have realized the bombshell they had dropped on the scientific world. Knowledge of the inner workings of proteins -- molecules often referred to as the building blocks of life -- would be the key to understanding biology at the molecular level" (Brownlee in PNAS Website). A full decade before x-ray crystallography first revealed the structures of proteins, Pauling and Corey deduced their main structural features: the alpha and the gamma helix. Their work had the same significance for proteins as the Watson and Crick papers, published two years later, had for the structure of DNA. In the short letter that published in this volume, the two scientists clearly state "that they had come up with two spiral models; they mention their hydrogen bonding scheme and assert that there was evidence that the proposed structures were present in a variety of proteins. They hinted at a molecular model for silk. They said nothing about the discrepancy between their models and the x-ray data. They ended with the promise that 'a detailed account of this work will be published soon'" (Special Collections and Archive Research, Oregon State). "Pauling and Corey's research, now over a half-century old, guides today's biotechnology revolution and the search for hundreds of disease cures -- drugs that may someday conquer Alzheimer's disease, cystic fibrosis, Mad Cow disease and many forms of cancer" (Brownlee). Linus Paulingwon the 1954 Nobel Prize in Chemistry "for his research into the nature of the chemical bond and its application to the elucidation of the structure of complex substances' (Nobel Prize Committee). CONDITION & DETAILS: Easton: American Chemical Society. Full volume. Quarto (10.25 x 7.5 inches; 256 x 188mm). Bound in maroon cloth with decorative paper boards. Gilt-lettered, green morocco spine label. Minor rubbing and scuffing at the edges. Tiny spot on spine label. Tightly and very solidly bound. Bright and clean throughout. Very good condition.

1st Edition. FIRST EDITION OF THREE OF SEVEN PAPERS BY PAULING AND COREY ON THE MOLECULAR STRUCTURE OF PROTEINS. A decade before x-ray crystallography first revealed the structures of proteins, Pauling and Corey deduced their main structural features: the 'alpha-helix,' the 'gamma helix' and the 'beta sheet.' Their work had the same significance for proteins as the Watson and Crick papers (published two years later) had for the structure of DNA. "Instead of tackling the structure of an entire protein, the two scientists' efforts centered on discrete bits of proteins -- tiny crystals made up of repeating units called amino acids. When numberous amino acids link together to form chains, the chains assemble into one of several different configurations. Because an entire protein can encompass hundreds of these configurations folded into a tangled and sometimes impenetrable bundle, Pauling and Corey focused on elucidating the structure of each configuration one by one" (Brownlee, 'The Protein Papers,' on the PNAS at 100: Classics of the Scientific Literature, PNAS Website). "Pauling and Corey's research, now over a half-century old, guides today's biotechnology revolution and the search for hundreds of disease cures" (ibid). Linus Pauling was awarded the Nobel Prize in Chemistry in 1954 "for his research into the nature of the chemical bond and its application to the elucidation of the structure of complex substances" (ibid). CONDITION & DETAILS: Easton, PA: National Academy of Sciences. Two volume first edition Proceedings of the National Academy of Sciences, Vol. 37 and 38, 1951. Entire volumes. Quarto. (10 x 7 inches; 250 x 175mm). Bound in dark tan buckram, gilt-lettered at the spine. Moderate surface rubbing and scuffing. Tightly and very solidly bound. Bright and very clean throughout. Very good condition.